CAND1_RAT
ID CAND1_RAT Reviewed; 1230 AA.
AC P97536;
DT 07-JUN-2005, integrated into UniProtKB/Swiss-Prot.
DT 01-MAY-1997, sequence version 1.
DT 03-AUG-2022, entry version 140.
DE RecName: Full=Cullin-associated NEDD8-dissociated protein 1;
DE AltName: Full=Cullin-associated and neddylation-dissociated protein 1;
DE AltName: Full=TBP-interacting protein of 120 kDa A;
DE Short=TBP-interacting protein 120A;
DE AltName: Full=p120 CAND1;
GN Name=Cand1; Synonyms=Tip120, Tip120a;
OS Rattus norvegicus (Rat).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC Murinae; Rattus.
OX NCBI_TaxID=10116;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA], PARTIAL PROTEIN SEQUENCE, INTERACTION WITH TBP,
RP AND SUBCELLULAR LOCATION.
RC TISSUE=Liver;
RX PubMed=8954946; DOI=10.1006/bbrc.1996.1852;
RA Yogosawa S., Makino Y., Yoshida T., Kishimoto T., Muramatsu M.,
RA Tamura T.-A.;
RT "Molecular cloning of a novel 120-kDa TBP-interacting protein.";
RL Biochem. Biophys. Res. Commun. 229:612-617(1996).
RN [2]
RP TISSUE SPECIFICITY.
RX PubMed=10441524; DOI=10.1006/bbrc.1999.1147;
RA Aoki T., Okada N., Ishida M., Yogosawa S., Makino Y., Tamura T.-A.;
RT "TIP120B: a novel TIP120-family protein that is expressed specifically in
RT muscle tissues.";
RL Biochem. Biophys. Res. Commun. 261:911-916(1999).
RN [3]
RP FUNCTION.
RX PubMed=10567521; DOI=10.1128/mcb.19.12.7951;
RA Makino Y., Yogosawa S., Kayukawa K., Coin F., Egly J.-M., Wang Z.-X.,
RA Roeder R.G., Yamamoto K., Muramatsu M., Tamura T.-A.;
RT "TATA-Binding protein-interacting protein 120, TIP120, stimulates three
RT classes of eukaryotic transcription via a unique mechanism.";
RL Mol. Cell. Biol. 19:7951-7960(1999).
RN [4]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-335 AND SER-558, AND
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=22673903; DOI=10.1038/ncomms1871;
RA Lundby A., Secher A., Lage K., Nordsborg N.B., Dmytriyev A., Lundby C.,
RA Olsen J.V.;
RT "Quantitative maps of protein phosphorylation sites across 14 different rat
RT organs and tissues.";
RL Nat. Commun. 3:876-876(2012).
CC -!- FUNCTION: Key assembly factor of SCF (SKP1-CUL1-F-box protein) E3
CC ubiquitin ligase complexes that promotes the exchange of the substrate-
CC recognition F-box subunit in SCF complexes, thereby playing a key role
CC in the cellular repertoire of SCF complexes. Acts as a F-box protein
CC exchange factor. The exchange activity of CAND1 is coupled with cycles
CC of neddylation conjugation: in the deneddylated state, cullin-binding
CC CAND1 binds CUL1-RBX1, increasing dissociation of the SCF complex and
CC promoting exchange of the F-box protein. Probably plays a similar role
CC in other cullin-RING E3 ubiquitin ligase complexes (By similarity). May
CC indirectly enhance transcription from various types of promoters.
CC {ECO:0000250, ECO:0000269|PubMed:10567521}.
CC -!- SUBUNIT: Interacts with TBP (PubMed:8954946). Part of a complex that
CC contains CUL1 and RBX1. Interacts with unneddylated cullins: interacts
CC with CUL1, CUL2, CUL3, CUL4A, CUL4B and CUL5. Does not bind neddylated
CC CUL1. Interaction with cullins is abolished in presence of COMMD1,
CC which antagonizes with CAND1 for interacting with cullins. Interacts
CC with ERCC6 (By similarity). Interacts with DCUN1D1, DCUN1D2, DCUN1D3,
CC DCUN1D4 AND DCUN1D5; these interactions are bridged by cullins and
CC strongly inhibits the neddylation of cullins (By similarity).
CC {ECO:0000250|UniProtKB:Q86VP6, ECO:0000269|PubMed:8954946}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250|UniProtKB:Q86VP6}. Nucleus
CC {ECO:0000250|UniProtKB:Q86VP6}. Note=Predominantly cytoplasmic.
CC {ECO:0000250|UniProtKB:Q86VP6}.
CC -!- TISSUE SPECIFICITY: Detected in heart, brain, spleen, liver, skeletal
CC muscle, kidney and testis. {ECO:0000269|PubMed:10441524}.
CC -!- SIMILARITY: Belongs to the CAND family. {ECO:0000305}.
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DR EMBL; D87671; BAA13432.1; -; mRNA.
DR PIR; T42735; T42735.
DR RefSeq; NP_446456.1; NM_054004.2.
DR AlphaFoldDB; P97536; -.
DR SMR; P97536; -.
DR BioGRID; 250683; 6.
DR IntAct; P97536; 3.
DR MINT; P97536; -.
DR STRING; 10116.ENSRNOP00000010720; -.
DR iPTMnet; P97536; -.
DR PhosphoSitePlus; P97536; -.
DR jPOST; P97536; -.
DR PaxDb; P97536; -.
DR PRIDE; P97536; -.
DR Ensembl; ENSRNOT00000010720; ENSRNOP00000010720; ENSRNOG00000007834.
DR GeneID; 117152; -.
DR KEGG; rno:117152; -.
DR UCSC; RGD:620479; rat.
DR CTD; 55832; -.
DR RGD; 620479; Cand1.
DR eggNOG; KOG1824; Eukaryota.
DR GeneTree; ENSGT00390000017740; -.
DR HOGENOM; CLU_007157_0_0_1; -.
DR InParanoid; P97536; -.
DR OMA; MGGTQDD; -.
DR OrthoDB; 194023at2759; -.
DR PhylomeDB; P97536; -.
DR Reactome; R-RNO-6798695; Neutrophil degranulation.
DR Reactome; R-RNO-8951664; Neddylation.
DR Reactome; R-RNO-917937; Iron uptake and transport.
DR PRO; PR:P97536; -.
DR Proteomes; UP000002494; Chromosome 7.
DR Bgee; ENSRNOG00000007834; Expressed in thymus and 19 other tissues.
DR Genevisible; P97536; RN.
DR GO; GO:0031461; C:cullin-RING ubiquitin ligase complex; ISS:UniProtKB.
DR GO; GO:0005737; C:cytoplasm; ISS:UniProtKB.
DR GO; GO:0005829; C:cytosol; IEA:Ensembl.
DR GO; GO:0005794; C:Golgi apparatus; IEA:Ensembl.
DR GO; GO:0005654; C:nucleoplasm; IEA:Ensembl.
DR GO; GO:0005634; C:nucleus; IDA:RGD.
DR GO; GO:0000151; C:ubiquitin ligase complex; ISS:UniProtKB.
DR GO; GO:0017025; F:TBP-class protein binding; IDA:RGD.
DR GO; GO:0030154; P:cell differentiation; ISS:UniProtKB.
DR GO; GO:0043086; P:negative regulation of catalytic activity; ISS:UniProtKB.
DR GO; GO:0045899; P:positive regulation of RNA polymerase II transcription preinitiation complex assembly; IDA:UniProtKB.
DR GO; GO:0045893; P:positive regulation of transcription, DNA-templated; IDA:UniProtKB.
DR GO; GO:0016567; P:protein ubiquitination; ISS:UniProtKB.
DR GO; GO:0010265; P:SCF complex assembly; ISS:UniProtKB.
DR Gene3D; 1.25.10.10; -; 1.
DR InterPro; IPR011989; ARM-like.
DR InterPro; IPR016024; ARM-type_fold.
DR InterPro; IPR039852; CAND1/CAND2.
DR InterPro; IPR013932; TATA-bd_TIP120.
DR PANTHER; PTHR12696; PTHR12696; 1.
DR Pfam; PF08623; TIP120; 1.
DR SUPFAM; SSF48371; SSF48371; 1.
PE 1: Evidence at protein level;
KW Acetylation; Cytoplasm; Direct protein sequencing; Nucleus; Phosphoprotein;
KW Reference proteome; Repeat; Transcription; Transcription regulation;
KW Ubl conjugation pathway.
FT INIT_MET 1
FT /note="Removed"
FT /evidence="ECO:0000250|UniProtKB:Q86VP6"
FT CHAIN 2..1230
FT /note="Cullin-associated NEDD8-dissociated protein 1"
FT /id="PRO_0000089296"
FT REPEAT 2..39
FT /note="HEAT 1"
FT REPEAT 44..81
FT /note="HEAT 2"
FT REPEAT 83..119
FT /note="HEAT 3"
FT REPEAT 131..165
FT /note="HEAT 4"
FT REPEAT 171..208
FT /note="HEAT 5"
FT REPEAT 210..247
FT /note="HEAT 6"
FT REPEAT 248..282
FT /note="HEAT 7"
FT REPEAT 289..366
FT /note="HEAT 8"
FT REPEAT 370..407
FT /note="HEAT 9"
FT REPEAT 424..467
FT /note="HEAT 10"
FT REPEAT 471..510
FT /note="HEAT 11"
FT REPEAT 515..552
FT /note="HEAT 12"
FT REPEAT 563..602
FT /note="HEAT 13"
FT REPEAT 606..643
FT /note="HEAT 14"
FT REPEAT 646..683
FT /note="HEAT 15"
FT REPEAT 688..725
FT /note="HEAT 16"
FT REPEAT 729..768
FT /note="HEAT 17"
FT REPEAT 770..808
FT /note="HEAT 18"
FT REPEAT 809..845
FT /note="HEAT 19"
FT REPEAT 852..889
FT /note="HEAT 20"
FT REPEAT 890..927
FT /note="HEAT 21"
FT REPEAT 928..960
FT /note="HEAT 22"
FT REPEAT 961..998
FT /note="HEAT 23"
FT REPEAT 1002..1039
FT /note="HEAT 24"
FT REPEAT 1043..1097
FT /note="HEAT 25"
FT REPEAT 1099..1133
FT /note="HEAT 26"
FT REPEAT 1140..1189
FT /note="HEAT 27"
FT REGION 315..344
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 315..342
FT /note="Acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 2
FT /note="N-acetylalanine"
FT /evidence="ECO:0000250|UniProtKB:Q86VP6"
FT MOD_RES 55
FT /note="N6-acetyllysine"
FT /evidence="ECO:0000250|UniProtKB:Q86VP6"
FT MOD_RES 335
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:22673903"
FT MOD_RES 558
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:22673903"
FT MOD_RES 971
FT /note="N6-acetyllysine"
FT /evidence="ECO:0000250|UniProtKB:Q86VP6"
SQ SEQUENCE 1230 AA; 136362 MW; A3ACF0E99B99A1D7 CRC64;
MASASYHISN LLEKMTSSDK DFRFMATNDL MTELQKDSIK LDDDSERKVV KMILKLLEDK
NGEVQNLAVK CLGPLVSKVK EYQVETIVDT LCTNMLSDKE QLRDISSIGL KTVIGELPPA
SSGSALAANV CKKITGRLTS AIAKQEDVSV QLEALDIMAD MLSRQGGLLV NFHPSILTCL
LPQLTSPRLA VRKRTIIALG HLVMSCGNIV FVDLIEHLLS ELSKNDSMST TRTYIQCIAA
ISRQAGHRIG EYLEKIIPLV VKFCNVDDDE LREYCIQAFE SFVRRCPKEV YPHVSTIINI
CLKYLTYDPN YNYDDEDEDE NAMDADGGDD DDQGSDDEYS DDDDMSWKVR RAAAKCLDAV
VSTRHEMLPE FYKTVSPALI SRFKEREENV KADVFHAYLS LLKQTRPVQS WLCDPDAMEQ
GETPLTMLQS QVPNIVKALH KQMKEKSVKT RQCCFNMLTE LVNVLPGALT QHIPVLVPGI
IFSLNDKSSS SNLKIDALSC LYVILCNHSP QVFHPHVQAL VPPVVACVGD PFYKITSEAL
LVTQQLVKVI RPLDQPSSFD ATPYIKDLFT CTIKRLKAAD IDQEVKERAI SCMGQIICNL
GDNLGPDLSN TLQIFLERLK NEITRLTTVK ALTLIAGSPL KIDLRPVLGE GVPILASFLR
KNQRALKLGT LSALDILIKN YSDSLTAAMI DAVLDELPPL ISESDMHVSQ MAISFLTTLA
KVYPSSLSKI SGSILNELIG LVRSPLLQGG ALSAMLDFFQ ALVVTGTNNL GYMDLLRMLT
GPVYSQSTAL THKQSYYSIA KCVAALTRAC PKEGPAVVGQ FIQDVKNSRS TDSIRLLALL
SLGEVGHHID LSGQLELKSV ILEAFSSPSE EVKSAASYAL GSISVGNLPE YLPFVLQEIT
SQPKRQYLLL HSLKEIISSA SVVGLKPYVE NIWALLLKHC ECAEEGTRNV VAECLGKLTL
IDPETLLPRL KGYLISGSSY ARSSVVTAVK FTISDHPQPI DPLLKNCIGD FLKTLEDPDL
NVRRVALVTF NSAAHNKPSL IRDLLDSVLP HLYNETKVRK ELIREVEMGP FKHTVDDGLD
IRKAAFECMY TLLDSCLDRL DIFEFLNHVE DGLKDHYDIK MLTFLMLVRL STLCPSAVLQ
RLDRLVEPLR ATCTTKVKAN SVKQEFEKQD ELKRSAMRAV AALLTIPEAE KSPLMSEFQS
QISSNPELAA IFESIQKDSS STNLESMDTS
